Harter C, Draken E, Lottspeich F, Wieland F T
Institute of Biochemistry I, University of Heidelberg, Germany.
FEBS Lett. 1993 Oct 11;332(1-2):71-3. doi: 10.1016/0014-5793(93)80487-f.
The homologue of the mammalian coatomer complex was isolated from yeast cytosol and separated on a modified urea-containing SDS-polyacrylamide gel system. An additional band in the 100 kDa molecular weight range appeared when compared to the protein pattern obtained in conventional Laemmli gels, exactly as observed for mammalian coatomer. Cross-reactivity with an anti-peptide antibody raised against the C-terminus of beta'-COP from bovine, and N-terminal sequence analysis, revealed that this protein from yeast is related to beta'-COP from mammals.
从酵母细胞质中分离出哺乳动物衣被蛋白复合物的同源物,并在改良的含尿素SDS聚丙烯酰胺凝胶系统上进行分离。与传统Laemmli凝胶中获得的蛋白质图谱相比,在100 kDa分子量范围内出现了一条额外的条带,这与在哺乳动物衣被蛋白中观察到的情况完全相同。与针对牛β'-COP C末端产生的抗肽抗体的交叉反应以及N端序列分析表明,酵母中的这种蛋白质与哺乳动物的β'-COP相关。